| MWexperimental | 34 | kDa |
| MWexpected | 31 | kDa |
| VPorod | 59 | nm3 |
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log I(s)
3.28×10-1
3.28×10-2
3.28×10-3
3.28×10-4
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s, nm-1
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Conformational signatures induced by ubiquitin modification in the amyloid-associated tau repeat domain
Gabriele Giachin.SASDV76 – Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to two Ubiquitins at tau residues C311 and C317
Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)Polyubiquitin-B
Polyubiquitin-B
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Fits and models
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Rg, nm
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Synchrotron SAXS data from solutions of microtubule-associated protein tau (lysine-rich four-repeat domain 4RD) synthetically linked to two ubiquitins at tau amino acids C311 and C317 in 100 mM NaCl, pH 6.8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123972 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 8.00 mg/ml was measured at 20°C. 20 successive 0.050 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
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